Two interaction modes of the gp41-derived peptides with gp41 and their correlation with antimembrane fusion activity |
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| Authors: | Ryu J R Jin B S Suh M J Yoo Y S Yoon S H Woo E R Yu Y G |
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| Institution: | Structural Biology Center, Bioanalysis and Biotransformation Research Center, Medicinal Chemistry Research Center, Korea Institute of Science and Technology, PO Box 131, Cheongryang, Seoul, 130-650, Korea. |
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| Abstract: | Peptides derived from gp41 effectively block the gp41-mediated cell fusion or HIV infection. A 36-mer (naDP178), 51-mer (C51) and 27-mer peptide (C27) from the membrane proximal region of gp41 have been examined their interaction modes with the coiled-coil motif of gp41 presented in thioredoxin (Trx-N) or the bacterially expressed ectodomain of gp41 (Ec-gp41ec). All of these peptides effectively inhibited the gp41-mediated membrane fusion, however, they showed distinct interaction modes with Ec-gp41ec or Trx-N. C51 peptide bound tightly to Trx-N, and it increased the solubility of Ec-gp41ec. naDP178 showed very weak binding affinity to Trx-N, however, it effectively solubilized Ec-gp41ec. In contrast, C27 peptide showed significant binding to Trx-N; however, it did not affect the solubility of Ec-gp41ec. These interaction modes of C-peptides were assumed to be related to their different inhibitory mechanism against gp41-mediated cell fusion. |
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